The condensing effect of glucagon on phospholipid bilayers
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Glucagon forms discoidal particles with dimyristoylphosphatidylcholine at temperatures below the phase transition. Under these conditions and at a lipid to protein molar ratio of 20 : 1, glucagon is observed to induce a closer packing of the phospholipid bilayer. Similar effects are observed upon the interaction of glucagon with dilauroylphosphatidylcholine. In the region of the phase transition the discoidal particles are observed by freeze-fracture electron microscopy to undergo end-to-end association leading to the formation of multilamellar structures containing only a few layers and having a large internal volume. Above the phase transition temperature the properties of the lipid appear to be unperturbed by glucagon according to either freeze-fracture or densitometer studies. These results support the importance of phospholipid phase transitions in peptide-lipid interactions.
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